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The intrinsic flexibility of the Kv voltage sensor and its implications for channel gating.

Abstract:

Analysis of the crystal structures of the intact voltage-sensitive potassium channel KvAP (from Aeropyrum pernix) and Kv1.2 (from rat brain), along with the isolated voltage sensor (VS) domain from KvAP, raises the question of the exact nature of the voltage-sensing conformational change that triggers activation of Kv and related voltage-gated channels. Molecular dynamics simulations of the isolated VS of KvAP in a detergent micelle environment at two different temperatures (300 K and 368 K) ...

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Publication status:
Published

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Publisher copy:
10.1529/biophysj.105.072199
Journal:
Biophysical journal More from this journal
Volume:
90
Issue:
5
Pages:
1598-1606
Publication date:
2006-03-01
DOI:
EISSN:
1542-0086
ISSN:
0006-3495
Language:
English
Keywords:
Pubs id:
pubs:100676
UUID:
uuid:894fd5b2-8223-4af0-9b74-c65afdb13a3e
Local pid:
pubs:100676
Source identifiers:
100676
Deposit date:
2012-12-19

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